Designing substrate specificity by protein engineering of electrostatic interactions.
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Rational approaches to improving selectivity in drug designThe crystal structure of recombinant rat pancreatic RNase AStructural, kinetic, and thermodynamic studies of specificity designed HIV-1 proteaseComparison of complexes formed by a crustacean and a vertebrate trypsin with bovine pancreatic trypsin inhibitor - the key to achieving extreme stability?An additional electrostatic interaction between adrenodoxin and P450c27 (CYP27A1) results in tighter binding than between adrenodoxin and p450scc (CYP11A1)Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papainSupracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kineticsRecombining low homology, functionally rich regions of bacterial subtilisins by combinatorial fragment exchangeStructural basis of substrate specificity in the serine proteasesProtein regions important for plasminogen activation and inactivation of alpha2-antiplasmin in the surface protease Pla of Yersinia pestis.Generation of a broad esterolytic subtilisin using combined molecular evolution and periplasmic expression.Characterizing structural features of cuticle-degrading proteases from fungi by molecular modeling.Structural and energetic determinants of the S1-site specificity in serine proteases.Phosphorylation of synthetic random polypeptides by protein kinase P and other protein-serine (threonine) kinases and stimulation or inhibition of kinase activities by microbial toxins.Electrostatic complementarity within the substrate-binding pocket of trypsinThermodynamic analysis of water molecules at the surface of proteins and applications to binding site prediction and characterization.Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering.Plasmodium subtilisin-like protease 1 (SUB1): insights into the active-site structure, specificity and function of a pan-malaria drug target.Engineering multiple properties of a protein by combinatorial mutagenesis.Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMRA streptavidin mutant with altered ligand-binding specificitySwitching substrate preference of thermophilic xylose isomerase from D-xylose to D-glucose by redesigning the substrate binding pocket.Constructing manmade enzymes for oxygen activation.Stabilizing biocatalysts.Restriction of substrate specificity of subtilisin E by introduction of a side chain into a conserved glycine residue.The complete amino acid substitutions at position 131 that are positively involved in cold adaptation of subtilisin BPN'.Protein engineering. The design, synthesis and characterization of factitious proteins.A novel member of the subtilisin-like protease family from Streptomyces albogriseolus.Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase.Pro-subtilisin E: purification and characterization of its autoprocessing to active subtilisin E in vitro.Contribution of interactions with the core domain of hirudin to the stability of its complex with thrombin.Interaction of semisynthetic variants of RNase A with ribonuclease inhibitor.Amino acid residues in the CDC25 guanine nucleotide exchange factor critical for interaction with RasIdentification of electrostatic interaction sites between the regulatory and catalytic subunits of cyclic AMP-dependent protein kinase.Use of calcium dependence as a means to study the interaction between growth hormones and their binding proteins in rabbit liver.The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket.A remodelled protease that cleaves phosphotyrosine substrates.Variation in the P2-S2 stereochemical selectivity towards the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin.Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.Structural determinants of specificity in the cysteine protease cruzain.
P2860
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P2860
Designing substrate specificity by protein engineering of electrostatic interactions.
description
1987 nî lūn-bûn
@nan
1987 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի մարտին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Designing substrate specificity by protein engineering of electrostatic interactions.
@ast
Designing substrate specificity by protein engineering of electrostatic interactions.
@en
Designing substrate specificity by protein engineering of electrostatic interactions.
@nl
type
label
Designing substrate specificity by protein engineering of electrostatic interactions.
@ast
Designing substrate specificity by protein engineering of electrostatic interactions.
@en
Designing substrate specificity by protein engineering of electrostatic interactions.
@nl
prefLabel
Designing substrate specificity by protein engineering of electrostatic interactions.
@ast
Designing substrate specificity by protein engineering of electrostatic interactions.
@en
Designing substrate specificity by protein engineering of electrostatic interactions.
@nl
P2093
P2860
P356
P1476
Designing substrate specificity by protein engineering of electrostatic interactions.
@en
P2093
P2860
P304
P356
10.1073/PNAS.84.5.1219
P407
P577
1987-03-01T00:00:00Z